Magnesium in PDB 3sni: Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors

All present enzymatic activity of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors:
3.1.4.17; 3.1.4.35;

The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sni was solved by M.S.Malamas, Y.Ni, J.Erdei, H.Stange, R.Schindler, H.-J.Lankau, C.Grunwald, K.Y.Fan, K.D.Parris, B.Langen, U.Egerland, T.Hage, K.L.Marquis, S.Grauer, J.Brennan, R.Navarra, R.Graf, B.L.Harrison, A.Robichaud, T.Kronbach, M.Pangalos, N.Hofgen, N.J.Brandon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.74 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.245, 81.337, 157.415, 90.00, 90.00, 90.00
R / Rfree (%)	24.7 / 31.9

The structure of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Magnesium atom in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors (pdb code 3sni). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors, PDB code: 3sni:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg781 b:14.0 occ:1.00 O A:HOH261 1.8 21.1 1.0 OD1 A:ASP554 1.9 24.5 1.0 O A:HOH89 1.9 32.8 1.0 O A:HOH72 2.1 13.3 1.0 O A:HOH43 2.3 14.1 1.0 O A:HOH92 2.3 24.3 1.0 CG A:ASP554 3.0 26.1 1.0 OD2 A:ASP554 3.5 21.9 1.0 ZN A:ZN780 3.8 34.0 1.0 OE2 A:GLU582 3.8 29.2 1.0 NE2 A:HIS585 4.0 27.3 1.0 O A:HIS553 4.0 25.2 1.0 O A:HOH110 4.1 23.1 1.0 CD2 A:HIS557 4.1 31.4 1.0 OG1 A:THR623 4.1 24.9 1.0 CD2 A:HIS585 4.2 27.8 1.0 NE2 A:HIS557 4.2 31.5 1.0 CB A:ASP554 4.3 26.4 1.0 CD2 A:HIS553 4.3 21.5 1.0 O A:HOH2 4.5 34.5 1.0 O A:THR623 4.6 26.0 1.0 CA A:ASP554 4.6 26.8 1.0 CD2 A:HIS515 4.6 26.9 1.0 O A:HOH111 4.7 15.6 1.0 OD2 A:ASP664 4.7 20.1 1.0 CD A:GLU582 4.7 29.8 1.0 CB A:THR623 4.8 24.9 1.0 NE2 A:HIS515 4.8 27.3 1.0 CG A:GLU582 4.8 30.4 1.0 NE2 A:HIS553 4.8 19.6 1.0 C A:HIS553 4.9 25.3 1.0

Magnesium binding site 2 out of 2 in the Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Highly Potent, Selective, and Orally Active Phosphodiestarase 10A Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg781 b:32.9 occ:1.00 O B:HOH25 2.0 20.6 1.0 O B:HOH50 2.1 43.5 1.0 OD1 B:ASP554 2.2 31.3 1.0 O B:HOH82 2.4 22.9 1.0 O B:HOH263 2.6 39.1 1.0 CG B:ASP554 3.2 32.4 1.0 OD2 B:ASP554 3.5 31.9 1.0 OE2 B:GLU582 3.8 52.5 1.0 ZN B:ZN780 3.9 34.2 1.0 OG1 B:THR623 4.1 42.2 1.0 NE2 B:HIS585 4.2 45.1 1.0 CD2 B:HIS553 4.3 29.8 1.0 O B:THR623 4.3 42.3 1.0 O B:HOH100 4.4 31.1 1.0 CD2 B:HIS557 4.4 41.0 1.0 O B:HIS553 4.5 31.5 1.0 CD2 B:HIS585 4.5 45.1 1.0 OD2 B:ASP664 4.5 29.5 1.0 CB B:ASP554 4.6 32.7 1.0 CB B:THR623 4.6 42.0 1.0 NE2 B:HIS557 4.7 40.8 1.0 NE2 B:HIS553 4.7 30.1 1.0 CD B:GLU582 4.8 52.4 1.0 NE2 B:HIS515 4.8 27.3 1.0 CD2 B:HIS515 4.8 27.3 1.0 CA B:ASP554 4.8 32.7 1.0 CG B:GLU582 5.0 52.2 1.0

M.S.Malamas, Y.Ni, J.Erdei, H.Stange, R.Schindler, H.J.Lankau, C.Grunwald, K.Y.Fan, K.Parris, B.Langen, U.Egerland, T.Hage, K.L.Marquis, S.Grauer, J.Brennan, R.Navarra, R.Graf, B.L.Harrison, A.Robichaud, T.Kronbach, M.N.Pangalos, N.Hoefgen, N.J.Brandon. Highly Potent, Selective, and Orally Active Phosphodiesterase 10A Inhibitors. J.Med.Chem. V. 54 7621 2011.
ISSN: ISSN 0022-2623
PubMed: 21988093
DOI: 10.1021/JM2009138